Warning: Undefined variable $zfal in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Deprecated: str_replace(): Passing null to parameter #3 ($subject) of type array|string is deprecated in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 525
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 530
Warning: Undefined variable $sterm in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 531
Warning: file_get_contents(http://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=14527663&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests
in C:\Inetpub\vhosts\kidney.de\httpdocs\mlpefetch.php on line 445
 
English Wikipedia
Nephropedia Template TP (
Twit Text
DeepDyve
Pubget Overpricing |  
lüll
The gelsolin family of actin regulatory proteins: modular structures, versatile functions McGough AM; Staiger CJ; Min JK; Simonetti KDFEBS Lett 2003[Sep]; 552 (2-3): 75-81This issue of FEBS Letters includes two manuscripts describing structural studies of gelsolin, the best-characterized member of a superfamily of actin binding proteins that sever, cap, and in some cases nucleate and bundle actin filaments. The manuscripts by Narayan et al. and Irobi et al. provide snapshots of gelsolin domains activated by calcium and in complex with the actin monomer, revealing new insights into the remarkable actin regulatory activities of this versatile protein. These studies build upon nearly a quarter of a century of research on gelsolin's effects on actin dynamics and its role in normal and diseased cells. In the following minireview, we summarize the structural studies that have provided insights into gelsolin's severing and capping activities and look to the future of work on this remarkable molecule.|Actins/metabolism[MESH]|Animals[MESH]|Calcium/metabolism[MESH]|Cryoelectron Microscopy[MESH]|Crystallography, X-Ray[MESH]|Gelsolin/*chemistry/*physiology[MESH]|Humans[MESH]|Models, Molecular[MESH]|Molecular Structure[MESH]|Nuclear Magnetic Resonance, Biomolecular[MESH]|Protein Binding[MESH]|Protein Structure, Tertiary[MESH] |
